ID A0A1F4K3A6_9BURK Unreviewed; 338 AA.
AC A0A1F4K3A6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:OGB29131.1};
GN ORFNames=A3F78_15205 {ECO:0000313|EMBL:OGB29131.1};
OS Burkholderiales bacterium RIFCSPLOWO2_12_FULL_61_40.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX NCBI_TaxID=1797566 {ECO:0000313|EMBL:OGB29131.1, ECO:0000313|Proteomes:UP000178940};
RN [1] {ECO:0000313|EMBL:OGB29131.1, ECO:0000313|Proteomes:UP000178940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU361277};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000256|RuleBase:RU361277}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGB29131.1}.
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DR EMBL; MESI01000115; OGB29131.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F4K3A6; -.
DR STRING; 1797566.A3F78_15205; -.
DR Proteomes; UP000178940; Unassembled WGS sequence.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd05283; CAD1; 1.
DR Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH-like_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR047109; CAD-like.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR PANTHER; PTHR42683; ALDEHYDE REDUCTASE; 1.
DR PANTHER; PTHR42683:SF38; ALDEHYDE REDUCTASE AHR; 1.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; GroES-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|RuleBase:RU361277};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Zinc {ECO:0000256|RuleBase:RU361277}.
FT DOMAIN 14..333
FT /note="Enoyl reductase (ER)"
FT /evidence="ECO:0000259|SMART:SM00829"
SQ SEQUENCE 338 AA; 36409 MW; E55D74113B30959A CRC64;
MTQFRAWAAT RSGGPLEKFE FDPGPMDPED VEIAVEYCGV CHSDLAMVDS EWFPANYPLV
PGHEVVGTIV AVGAQAKGRH VGQRVGLGWH SRSCLHCQHC LGGEQNLCRK SQPTIIGRHG
GFADRVRAHW SWNIPLPDAL DASAVGPLMC GGGTAFLPFV VHGIQPTDKV GVVGIGGLGH
LAVKFARAWG CEVTAFTSTP SKREEALALG AHHTISSVDV KELKTIAGTL DFLLVTVGAS
LEWDALIGTL APKGRMHMVG VVTEAMKLRT SGLLSWQRSI SASPTPSPTM LAKMLEFSAR
HGIAPQVEHF PMRRVNEALD HLRSGQARYR VVLDADFS
//
